ID A0A178EK82_9PLEO Unreviewed; 2116 AA.
AC A0A178EK82;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN ORFNames=IQ07DRAFT_499742 {ECO:0000313|EMBL:OAL56055.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL56055.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL56055.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL56055.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000256|ARBA:ARBA00004134}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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DR EMBL; KV441637; OAL56055.1; -; Genomic_DNA.
DR STRING; 765867.A0A178EK82; -.
DR InParanoid; A0A178EK82; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR CDD; cd11858; SH3_Myosin-I_fungi; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035535; Fungal_myosin-I_SH3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF837; MYOSIN-3-RELATED; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF82615; Polo-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50078; POLO_BOX; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361162};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU361162};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361162}.
FT DOMAIN 23..297
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 738..759
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT DOMAIN 906..1585
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1643..1833
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1939..2020
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1480
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1801..1942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2021..2095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1923..1941
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2021..2036
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2067..2084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 999..1006
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2116 AA; 235924 MW; 4AE22C73777FD0E2 CRC64;
MSAPSIHADA PPAIVQDPEG LQYETGPQLG KGGFAICHRA KLLGHEHLGS STVALKIVRS
KMEPPKLAQK ARFSQQLDFV TELQIHSKLS HPNIVEFYRA FSFETSTYVV LELCENGSLA
DAIKKRKYFT MPEIRRFMIQ TCGAIKYLHQ RNIVHRDLKT GNLFLDKDMN VKVGDFGLAA
LLVSQSDFGA IRRTTMCGTP NYLAPEVLEK TGKGHDEKVD IWAIGIMMYT LAVGRAPFHA
AKREDIYRKL KACEYTWPDL AKFANEITDD LRDIVSLLLV HEDDRPTPDL IVAHPFFRLG
YIPLELDSGC TSRIPKWPKN RPPTAATIKR GYTEDWWKLC KASAVGEYES GRSFGDHGHR
KNKSVAKDCQ REIVAGKQPS VPFSKDMVYV PYPARVQWPH QAPGGLSEIS EEKESSSEGQ
ALVETTGNDR QGGRLPRATR KEQPMPTLKE NTEPVQEPEL ARRTLDKQPT RLRAVRKISN
PGRITAATAT APAPLRVPRD SKTITRTRTA KDTVKEVPRA TETGLPDLPP LRVIKTNTRS
TERPETASQP KTVRSAARYR TLSAEMPSTD QVSVLARLYT FRDNLARALD KKPTKSRRDQ
PPHLPFVAKW VDYSRRYGVG YVLDDGSIGI LLSAEEHYPV TVAFATDGYS HLRKAGNNRE
LAKSVALEYY TTLKKERGLS QIEVLESRRI EEIRTVWHKF GKYMCATFGD EERPMRKDSR
VNFVKFYQRL GNVGIWGFDD GSFQFNFPDH TKLVLSSDAG YGHFLCLQQD GTDALGETGF
VPWKHVKVRE HLRGSLQQLL YGSADKEDSN RELTENNLLR TKIEFIYKVV EEWVQQGGLG
CLVDPKAYSW TGRQLEETKR LDWASAVTKR AGRKKDAGGS KAAGGGQQKS QFAKKAVFET
TKKKEVGVSD LTLISKISNE AINDNLKKRF ENGEIYTYIG HVLVSVNPFR DLGIYTDQVL
DSYKGKNRLE VPPHVFAIAE SSYYNMNAYK ENQCVIISGE SGAGKTEAAK RLMQYIASVS
GGSNSSIQEI KDMVLATNPL LESFGNAKTL RNNNSSRFGK YLEIHFNAQG EPVGANINNY
LLEKTRVVGQ ITNERNFHIF YQFTKAASPQ YREIFGLQQP QSYLYTSRSK CYDVQGIDDH
AEFQDTLNAM NIIGLQQAEQ DNIFRMLAAI LWLGNVSFRE DDTGNAAIVD QSVVDFVAYL
LEVDSAHVNK ALTIRIVETS RGGRRGSIYD VPLNCTQAGS VRDALAKAIY FNLFDWIVER
VNVSLKARGA TAHSIGILDI YGFEIFERNS FEQLCINYVN EKLQQIFIQL TLKAEQEEYE
REQIKWTPIK YFDNKVVCEL IEEKRPPGVF AALNDACATA HADPTAADQT FVQRLNALSS
NPNFQPRQGQ FVIKHYAGDV SYAIDGMTDK NKDQLLKDLL NLLGNSGNTF VHTLFPNQVD
QDNKRRPPTA GDKIKASAND LVTTLMQARP SYIRTIKPNE NKSPKEYNEP NVLHQIKYLG
LQENVRIRRA GFASRQTFDK FVERFFLLSP KCSYAGEYTW TGDYETGAKQ ILKDTNIPAE
EFQMGVTKVF IKTPETLFAL ETMRDRYWHN MAIRIQRAWR NYLRYRTECA IRIQRFWRRL
NGGKEFIELR DQGHKVLQGR KERRRYSLVG YRRFMGDYLG IGNRGGPGEV IANAIGVSAN
EEVPFSCRAE TLVSKLGRSS KPEPRTLVLT KRNVYLVKQV LVNRQVQIQA ERTIPVGAIK
FVSCSTLKDD WFSIGVGSPQ EPDPLVNCVF KTEFFTHLTN VLRGGLTLKI GDTIEYNKKP
GKPAQVKVVK DPAVQRDDLY KSGTVHTGPG EPPNSRSKAT PKGRQIAAKP ITKGKLLRPG
GPGGGPSKLA SRPAQPRPVP TPAASQARVV PQPAVSQPRA VPQPVAALSN GTGAHARTGS
ATRAAPPPPP SAPPAPAPPA EPTFKALYDF AGQSAGELSL KKDEIILITQ KENNGICTLV
YLHTKDTANS QLQTGWWLAS RLDKSASGWA PSAYLEEVIQ RAPAPPPPPP PPARPANGST
VGGKAKPPAP PAKRPAARKP VHSDSGRDSG YSGSGASMVD SGGARDSSGS IAGGLAEALR
QRQLAMQGKS RQEDDW
//
